ID   RL131_PLAVT             Reviewed;         158 AA.
AC   P0CU91;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Secreted RxLR effector protein 131 {ECO:0000303|PubMed:30945786};
DE   Flags: Precursor;
GN   Name=RXLR131 {ECO:0000303|PubMed:30945786};
OS   Plasmopara viticola (Downy mildew of grapevine) (Botrytis viticola).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Plasmopara.
OX   NCBI_TaxID=143451;
RN   [1]
RP   DOMAIN, INDUCTION, SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH
RP   HOST BKI1.
RX   PubMed=30945786; DOI=10.1111/mpp.12790;
RA   Lan X., Liu Y., Song S., Yin L., Xiang J., Qu J., Lu J.;
RT   "Plasmopara viticola effector PvRXLR131 suppresses plant immunity by
RT   targeting plant receptor-like kinase inhibitor BKI1.";
RL   Mol. Plant Pathol. 20:765-783(2019).
CC   -!- FUNCTION: Secreted effector that suppresses pathogen-associated
CC       molecular pattern (PAMP)-triggered immunity (PTI) in host plants
CC       (PubMed:30945786). Suppresses both defense-related brassinosteroid (BR)
CC       and ERECTA (ER) signaling pathways in planta by interacting with host
CC       BRI1 kinase inhibitor 1 (BKI1) at the host plasma membrane, leading to
CC       a host dwarf phenotype (PubMed:30945786).
CC       {ECO:0000269|PubMed:30945786}.
CC   -!- SUBUNIT: Interacts with host BKI1. {ECO:0000269|PubMed:30945786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30945786}. Host cell
CC       membrane {ECO:0000269|PubMed:30945786}; Single-pass type I membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is induced during infection of host grapevine.
CC       {ECO:0000269|PubMed:30945786}.
CC   -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC       cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC       phosphate. {ECO:0000305|PubMed:30945786}.
CC   -!- DOMAIN: The 39 amino acids in the C-terminus (residues 120 to 158) are
CC       sufficient for binding the host BKI1. {ECO:0000269|PubMed:30945786}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CU91; -.
DR   SMR; P0CU91; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host cell membrane; Host membrane; Membrane; Secreted;
KW   Signal; Transmembrane; Transmembrane helix; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..158
FT                   /note="Secreted RxLR effector protein 131"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000447964"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          120..158
FT                   /note="Host BKI1-binding"
FT                   /evidence="ECO:0000269|PubMed:30945786"
FT   MOTIF           39..57
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:30945786"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   158 AA;  17096 MW;  FC1ADEE38290D55A CRC64;
     MRQIPLVVVL LLAYAARLQG LISVTNAAVG AKPGPHAGRD LDGSTTSMSV NVDDEERGLS
     DMLKRLRSML FDANSATKGQ ALKKDAKSTK SVKAAGAASN AKKVGQLRHM WNQIKNVEYK
     GNVKYLAIIY VICILSVLGI LGTVFAINRN ISNQYIHE